Reviewed, UniProtKB/Swiss-Prot P56961 (ARODE_CHLMU)

Names and origin

Protein names

Recommended name:
    Shikimate biosynthesis protein aroDE
Including the following 2 domains:
    1- Recommended name:
            3-dehydroquinate dehydratase
                Short name=3-dehydroquinase
              EC=4.2.1.10
        Alternative name(s):
            Type I DHQase
    2- Recommended name:
            Shikimate dehydrogenase
              EC=1.1.1.25

Gene names

Name:	aroE
Synonyms:	aroD/E
Ordered Locus Names:	TC_0649

Organism

Chlamydia muridarum [Complete proteome] [HAMAP]

Taxonomic identifier

83560 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes two sequential steps of the aromatic amino acids biosynthetic pathway. The first reaction is catalyzed by the 3-dehydroquinate dehydratase, coded by the aroD domain; the second reaction is catalyzed by the shikimate 5-dehydrogenase, coded by the aroE domain. HAMAP MF_00214
Catalytic activity	3-dehydroquinate = 3-dehydroshikimate + H2O. HAMAP MF_00214 Shikimate + NADP+ = 3-dehydroshikimate + NADPH. HAMAP MF_00214
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. HAMAP MF_00214 Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Sequence similarities	In the N-terminal section; belongs to the type-I 3-dehydroquinase family. In the C-terminal section; belongs to the shikimate dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Ligand	NADP Schiff base
Molecular function	Lyase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	3-dehydroquinate dehydratase activity Inferred from electronic annotation. Source: HAMAP NADP or NADPH binding Inferred from electronic annotation. Source: InterPro shikimate 5-dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 478	478	Shikimate biosynthesis protein aroDE HAMAP MF_00214		PRO_0000138822
Regions
	Nucleotide binding	337 – 341	5	NADP By similarity
	Region	1 – 208	208	3-dehydroquinate dehydratase HAMAP MF_00214
	Region	209 – 478	270	Shikimate 5-dehydrogenase HAMAP MF_00214
Sites
	Active site	110	1	Proton acceptor By similarity
	Active site	133	1	Schiff-base intermediate with substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P56961-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 199EEF5251205AB9	FASTA	478	53,211
	10 20 30 40 50 60 MLCTIIRGPS FLEARNQLLR SLKKCRCFEM RADLLTVSDA ELQKLILLAP ISVLTWKKPP 70 80 90 100 110 120 SCTPQAWVKK IQSLAKLHPT YLDLDKDFPE EEILHIRHLH PNIKIIRSLH TSEHTDITQL 130 140 150 160 170 180 YTQMLASSID YYKLAVSPAS TTDLLNICRQ KHSLPQNTTV LCLGKIGQSS RILSPILQNP 190 200 210 220 230 240 FTYTIPTGAD PVAPGQLSLN HHYFYNFTNL SPQSQICALI GDTSRSIGHL THNPFFSQLS 250 260 270 280 290 300 IPCPYVKLPL TPQELPEFFS SIRALPFLGI SVTSPLKTAI IPFLDKQDSS VKLSGSCNTL 310 320 330 340 350 360 VIRQGEIIGY DTDGEGLFSV LTQHNMDLSN QRVAILGAGG AARSIAARLS RTGCELLIFN 370 380 390 400 410 420 RTKIHAEAIA SRYQAQAFDI KDLPLHSVSL IINCLPPSSI IPQALAPLIV DINTLPKHNS 430 440 450 460 470 FTQYARLKGC SIIYGHEMFA QQALLQFRLW FPTHSFNHLE KNFSRRAAVL ASLFSIAA

References

[1]

"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39." Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L. , Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M. Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MoPn / Nigg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002160 Genomic DNA. Translation: AAF39475.1.
PIR	G81679.
RefSeq	NP_297023.1.
3D structure databases
SMR	P56961. Positions 1-453.
ModBase	Search...
Genome annotation databases
GeneID	1246010.
GenomeReviews	Gene locus TC_0649 in contig AE002160_GR.
KEGG	cmu:TC0649.
TIGR	TC_0649.
Phylogenomic databases
HOGENOM	HBG414053.
OMA	ISHLSHN.
Enzyme and pathway databases
BioCyc	CMUR243161:TC_0649-MONOMER.
BRENDA	1.1.1.25. 256349. 4.2.1.10. 256349.
Family and domain databases
HAMAP	MF_00214. AroD. Fused. [Tree] MF_00222. Shikimate_DH_AroE. Fused. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR001381. DHquinase_I. IPR016040. NAD(P)-bd_dom. IPR011342. Quinate/shikimate_5-DH. IPR013708. Shikimate_DH-bd_N. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF01487. DHquinase_I. 1 hit. PF01488. Shikimate_DH. 1 hit. PF08501. Shikimate_dh_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00507. aroE. 1 hit.
PROSITE	PS01028. DEHYDROQUINASE_I. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARODE_CHLMU

Accession

Primary (citable) accession number: P56961

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	February 9, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)